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NCBI: 03-AUG-2016

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_01431
  • pan locus tag?: SAUPAN003854000
  • symbol: SAOUHSC_01431
  • pan gene symbol?: msrB
  • synonym:
  • product: methionine sulfoxide reductase B

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SAOUHSC_01431
  • symbol: SAOUHSC_01431
  • product: methionine sulfoxide reductase B
  • replicon: chromosome
  • strand: -
  • coordinates: 1368116..1368544
  • length: 429
  • essential: no DEG other strains

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

⊟DNA sequence[edit | edit source]

  • 1
    61
    121
    181
    241
    301
    361
    421
    ATGCTTAAAAAAGATAAAAGTGAACTAACAGATATAGAATATATTGTTACACAAGAAAAC
    GGCACTGAACCACCATTTATGAATGAATATTGGAATCATTTTGCTAAAGGAATTTATGTA
    GATAAAATTTCTGGTAAACCTTTATTTACATCTGAAGAAAAGTTTCATTCTGAATGTGGA
    TGGCCTAGCTTTTCCAAAGCGCTTGATGACGATGAAATTATAGAATTAGTCGACAAATCA
    TTTGGTATGTTGAGAACTGAAGTGCGTTCAGAAGAATCAAATAGTCATTTAGGACATGTC
    TTTAATGATGGACCTAAAGAAAGTGGCGGCTTAAGATACTGTATCAATTCCGCTGCAATT
    CAATTTATTCCATATGAAAAGTTAGAAGAATTGGGTTATGGCGATTTAATATCACATTTT
    GATAAGTAG
    60
    120
    180
    240
    300
    360
    420
    429

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SAOUHSC_01431
  • symbol: SAOUHSC_01431
  • description: methionine sulfoxide reductase B
  • length: 142
  • theoretical pI: 4.49255
  • theoretical MW: 16277.1
  • GRAVY: -0.601408

⊟Function[edit | edit source]

  • reaction:
    EC 1.8.4.11?  ExPASy
    Peptide-methionine (S)-S-oxide reductase Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin
    EC 1.8.4.12?  ExPASy
    Peptide-methionine (R)-S-oxide reductase Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
  • TIGRFAM:
    Cellular processes Cellular processes Adaptations to atypical conditions methionine-R-sulfoxide reductase (TIGR00357; EC 1.8.4.-; HMM-score: 191.5)
    Genetic information processing Protein fate Protein modification and repair methionine-R-sulfoxide reductase (TIGR00357; EC 1.8.4.-; HMM-score: 191.5)
  • TheSEED  :
    • Peptide methionine sulfoxide reductase MsrB (EC 1.8.4.12)
    Protein Metabolism Protein processing and modification Peptide methionine sulfoxide reductase  Peptide methionine sulfoxide reductase MsrB (EC 1.8.4.12)
  • PFAM:
    Beta-tent (CL0080) SelR; SelR domain (PF01641; HMM-score: 158.1)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 7.5
    • Cytoplasmic Membrane Score: 1.15
    • Cellwall Score: 0.62
    • Extracellular Score: 0.73
    • Internal Helices: 0
  • LocateP: Intracellular
    • Prediction by SwissProt Classification: Cytoplasmic
    • Pathway Prediction: No pathway
    • Intracellular possibility: 1
    • Signal peptide possibility: -1
    • N-terminally Anchored Score: 1
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.017153
    • TAT(Tat/SPI): 0.00034
    • LIPO(Sec/SPII): 0.00047
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MLKKDKSELTDIEYIVTQENGTEPPFMNEYWNHFAKGIYVDKISGKPLFTSEEKFHSECGWPSFSKALDDDEIIELVDKSFGMLRTEVRSEESNSHLGHVFNDGPKESGGLRYCINSAAIQFIPYEKLEELGYGDLISHFDK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas [1] [2]
  • protein localization:
  • quantitative data / protein copy number per cell:
  • interaction partners:

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator:

⊟Transcription pattern[edit | edit source]

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

⊟Protein stability[edit | edit source]

  • half-life: no data available

⊟Biological Material[edit | edit source]

⊟Mutants[edit | edit source]

⊟Expression vector[edit | edit source]

⊟lacZ fusion[edit | edit source]

⊟GFP fusion[edit | edit source]

⊟two-hybrid system[edit | edit source]

⊟FLAG-tag construct[edit | edit source]

⊟Antibody[edit | edit source]

⊟Other Information[edit | edit source]

You are kindly invited to share additional interesting facts.

⊟Literature[edit | edit source]

⊟References[edit | edit source]

  1. ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
    A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
    Proteomics: 2015, 15(21);3648-61
    [PubMed:26224020] [WorldCat.org] [DOI] (I p)
  2. ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
    A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
    Sci Rep: 2017, 7(1);9718
    [PubMed:28887440] [WorldCat.org] [DOI] (I e)
  3. ↑ 3.0 3.1 3.2 3.3 Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
    Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
    PLoS Genet: 2016, 12(4);e1005962
    [PubMed:27035918] [WorldCat.org] [DOI] (I e)

⊟Relevant publications[edit | edit source]

V K Singh, J Moskovitz, B J Wilkinson, R K Jayaswal
Molecular characterization of a chromosomal locus in Staphylococcus aureus that contributes to oxidative defence and is highly induced by the cell-wall-active antibiotic oxacillin.
Microbiology (Reading): 2001, 147(Pt 11);3037-45
[PubMed:11700354] [WorldCat.org] [DOI] (P p)Jackob Moskovitz, Vineet K Singh, Jesus Requena, Brian J Wilkinson, Radheshyam K Jayaswal, Earl R Stadtman
Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity.
Biochem Biophys Res Commun: 2002, 290(1);62-5
[PubMed:11779133] [WorldCat.org] [DOI] (P p)

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